Investigation of the Reduced High-Potential Iron−Sulfur Protein from Chromatium vinosum and Relevant Model Compounds: A Unified Picture of the Electronic Structure of [Fe4S4]2+ Systems through Magnetic and Optical Studies-Reference-Cited by-同舟云学术

Investigation of the Reduced High-Potential Iron−Sulfur Protein from Chromatium vinosum and Relevant Model Compounds: A Unified Picture of the Electronic Structure of [Fe4S4]2+ Systems through Magnetic and Optical Studies

Published:2003-09-24 Issue:21 Volume:42 Page:6824-6850
ISSN:0020-1669
Container-title:Inorganic Chemistry
language:en
Short-container-title:Inorg. Chem.

Author:

Lawson Daku Latévi M.¹,Pécaut Jacques¹,Lenormand-Foucaut Alix¹,Vieux-Melchior Béatrice¹,Iveson Peter¹,Jordanov Jeanne¹

Affiliation:

1. Service de Chimie Inorganique et Biologique, UMR 5046, Département de Recherche Fondamentale sur la Matière Condensée, CEA-Grenoble, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France

Publisher

American Chemical Society (ACS)

Subject

Inorganic Chemistry,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ic034494n

Reference82 articles.

1. Iron-Sulfur Clusters: Nature's Modular, Multipurpose Structures

2. Amino acid sequence of high-redox-potential ferredoxin (HiPIP) isozymes from the extremely halophilic purple phototrophic bacterium, Ectothiorhodospira halophila

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